Metals in metalloproteins plan key roles in protein structure and/or activity: small molecule binding/transport, substrate or cofactor binding, etc. Characterization of the metal centers provides crucial insight into biophysical and biochemical processes. These insights will prove invaluable in biomedicine and health care. Electron Magnetic Resonance (EMR) spectroscopy is potentially a unique and powerful tool for detecting and characterizing paramagnetic (metal) center in metalloproteins. Spin-physics of these metals -- high zero-field splittings, large nuclear quadrapoles and rapid relaxation -- make it difficult if not impossible to study these centers by "traditional" fields and frequencies (0.35 Tesla, 9.5 GHz). Very high field EMR with 10-25 times higher fields and frequencies promises to overcome these difficulties. The long-term goal is the characterization of paramagnetic centers in metalloproteins. Double resonance and pulsed techniques need to be developed. Work must be done on basic sensitivity and sample environs. The aim of Phase I is the development of requisite superconducting-magnet, field controls to support further stages for the research. Control is required for precision, multi-Tesla sweeps and actively- stable, fixed-field operation. This technology is not commercially available and prototype systems in academia are inadequate to the task.